The platelet isoform of phosphofructokinase (PFKP) is a rate‑limiting enzyme involved in glycolysis that serves an important role in various types of cancer. The aim of the present study was to explore the specific regulatory relationship between PFKP and non‑small cell lung cancer (NSCLC) progression. PFKP expression in NSCLC tissues and corresponding adjacent tissues was detected using reverse transcription‑quantitative polymerase chain reaction (RT‑qPCR) and immunohistochemical analysis. PFKP expression in human bronchial epithelial cells (16HBE) and NSCLC cells (H1299, H23 and A549) was also detected using RT‑qPCR. Cell proliferation was detected by Cell Counting Kit‑8 and colony formation assays. Transwell invasion and wound healing assays, and flow cytometry were used to detect cell invasion, migration and apoptosis, respectively. The expression levels of glycolysis‑associated enzymes (hexokinase‑2, lactate dehydrogenase A and glucose transporter‑1), epithelial‑mesenchymal transition‑related proteins (N‑cadherin, vimentin and E‑cadherin) and apoptosis‑related proteins (caspase‑3 and B‑cell lymphoma‑2) were detected by western blotting. Glucose uptake, lactate production and the adenosine trisphosphate/adenosine diphosphate ratio were measured using the corresponding kits. The results of the present study demonstrated that PFKP expression was upregulated in NSCLC tissues and cells, and PFKP expression was related to lymph node metastasis and histological grade. In addition, overexpression of PFKP inhibited cell apoptosis, and promoted proliferation, migration, invasion and glycolysis of H1299 cells, whereas knockdown of PFKP had the opposite effects. In conclusion, PFKP inhibited cell apoptosis, and promoted proliferation, migration, invasion and glycolysis of NSCLC cells; these findings may lay the foundation for novel treatments of NSCLC.
Keywords: PFKP; NSCLC; aerobic glycolysis; proliferation; EMT.